Plasminogen interaction with Trypanosoma cruzi

Almeida, Laura Lopes de; Vanegas, Gilmer; Calcagno, Marina; Concepción, Juan Luís; Avilán, Luisana

doi:10.1590/s0074-02762004000100011

Cited by 24 publications

(14 citation statements)

References 23 publications

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“…Besides L. mexic ana, surface plasminogen binding has also been demonstrated in several other parasites: T. cruzi [90], Trichomonas vaginalis [91], S. bovis [28, 61], and S. japonicum [27]. In most of them, enolase has been proposed as the plasminogen receptor.…”

Section: The Role Of Plasminogen/plasmin and Enolase In The Virulementioning

confidence: 99%

Enolase: A Key Player in the Metabolism and a Probable Virulence Factor of Trypanosomatid Parasites—Perspectives for Its Use as a Therapeutic Target

et al. 2011

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Glycolysis and glyconeogenesis play crucial roles in the ATP supply and synthesis of glycoconjugates, important for the viability and virulence, respectively, of the human-pathogenic stages of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania spp. These pathways are, therefore, candidate targets for antiparasite drugs. The glycolytic/gluconeogenic enzyme enolase is generally highly conserved, with similar overall fold and identical catalytic residues in all organisms. Nonetheless, potentially important differences exist between the trypanosomatid and host enzymes, with three unique, reactive residues close to the active site of the former that might be exploited for the development of new drugs. In addition, enolase is found both in the secretome and in association with the surface of Leishmania spp. where it probably functions as plasminogen receptor, playing a role in the parasite's invasiveness and virulence, a function possibly also present in the other trypanosomatids. This location and possible function of enolase offer additional perspectives for both drug discovery and vaccination.

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Section: The Role Of Plasminogen/plasmin and Enolase In The Virulementioning

confidence: 99%

Enolase: A Key Player in the Metabolism and a Probable Virulence Factor of Trypanosomatid Parasites—Perspectives for Its Use as a Therapeutic Target

et al. 2011

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“…The interactions of some bacterial and fungal pathogens with the plasminogenplasmin system have been the most studied, and in the case of group A Streptococci, Staphylococcus aureus, Yersinia pestis, Borrelia burgdorferi and Candida albicans the interaction with plasminogen has been shown to be involved in invasiveness within the host (Goguen et al, 2000;Lähteenmäki et al, 2001;Crowe et al, 2003). The protozoa Leishmania mexicana and Trypanosoma cruzi have been reported to bind plasminogen and also to enhance the activation of plasminogen by tissue-type plasminogen activator (t-PA) (Avilan et al, 2000;Almeida et al, 2004). In helminths, two plasminogen-binding proteins have been identified: enolase in Fasciola hepatica and Onchocerca volvulus and glyceraldehyde-3-phosphate dehydrogenase in O. volvulus (Jolodan et al, 2003;Bernal et al, 2004;Erttmann et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Schistosoma bovis: Plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument

Ramajo-Hernández

Pérez–Sánchez

Ramajo-Martín

et al. 2007

Experimental Parasitology

100

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Schistosoma bovis is a ruminant haematic parasite that lives for years in the mesenteric vessels of the host. The aim of this work was to investigate the ability of adult S. bovis worms to interact with plasminogen, a central component in the host fibrinolytic system. Confocal microscopy analysis revealed that plasminogen bound to the tegument surface of the male-but not female-S. bovis worms and that this binding was strongly dependent on lysine residues. It was also observed that a protein extract of the worm tegument (TG) had the capacity to generate plasmin and to enhance the plasmin generation by the tissue-type plasminogen activator. Proteomic analysis of the TG extract identified 10 plasminogen-binding proteins, among which the major ones were enolase, glyceraldehyde-3-phosphate dehydrogenase and actin. This study represents the first report about the binding of plasminogen to Schistosoma sp. proteins.

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“…They redifferentiate into trypomastigotes that are released upon cell rupture and disseminate through the bloodstream to infect new cells or are taken up by a triatomine bug (4). To invade the host and the susceptible host cells, the parasite has to pass barriers such as the extracellular matrix thanks to surface or secreted proteases degrading the extracellular matrix (5, 6). The parasite might also indirectly trigger degradation of the extracellular matrix by activating host proteases.…”

Section: Introductionmentioning

confidence: 99%

“…The parasite might also indirectly trigger degradation of the extracellular matrix by activating host proteases. One of these is plasmin (6), which is produced from plasminogen by the action of plasminogen activator (7). To do this, the parasite can bind soluble plasminogen to its surface (6, 8).…”

Section: Introductionmentioning

confidence: 99%

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The Ly49E Receptor Inhibits the Immune Control of Acute Trypanosoma cruzi Infection

et al. 2016

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The protozoan parasite Trypanosoma cruzi circulates in the blood upon infection and invades various cells. Parasites intensively multiply during the acute phase of infection and persist lifelong at low levels in tissues and blood during the chronic phase. Natural killer (NK) and NKT cells play an important role in the immune control of T. cruzi infection, mainly by releasing the cytokine IFN-γ that activates the microbicidal action of macrophages and other cells and shapes a protective type 1 immune response. The mechanisms by which immune cells are regulated to produce IFN-γ during T. cruzi infection are still incompletely understood. Here, we show that urokinase plasminogen activator (uPA) is induced early upon T. cruzi infection and remains elevated until day 20 post-infection. We previously demonstrated that the inhibitory receptor Ly49E, which is expressed, among others, on NK and NKT cells, is triggered by uPA. Therefore, we compared wild type (WT) to Ly49E knockout (KO) mice for their control of experimental T. cruzi infection. Our results show that young, i.e., 4- and 6-week-old, Ly49E KO mice control the infection better than WT mice, indicated by a lower parasite load and less cachexia. The beneficial effect of Ly49E depletion is more obvious in 4-week-old male than in female mice and weakens in 8-week-old mice. In young mice, the lower T. cruzi parasitemia in Ly49E KO mice is paralleled by higher IFN-γ production compared to their WT controls. Our data indicate that Ly49E receptor expression inhibits the immune control of T. cruzi infection. This is the first demonstration that the inhibitory Ly49E receptor can interfere with the immune response to a pathogen in vivo.

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Plasminogen interaction with Trypanosoma cruzi

Cited by 24 publications

References 23 publications

Enolase: A Key Player in the Metabolism and a Probable Virulence Factor of Trypanosomatid Parasites—Perspectives for Its Use as a Therapeutic Target

Enolase: A Key Player in the Metabolism and a Probable Virulence Factor of Trypanosomatid Parasites—Perspectives for Its Use as a Therapeutic Target

Schistosoma bovis: Plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument

The Ly49E Receptor Inhibits the Immune Control of Acute Trypanosoma cruzi Infection

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